Molecular dissection of interactions between Rad51 and members
of the recombination-repair group

J 2001

Molecular dissection of interactions between Rad51 and members of the recombination-repair group

KREJČÍ, Lumír, Jiří DAMBORSKÝ, B. THOMSEN, M. DUNO, C. BENDIXEN et. al.

Basic information

Original name

Molecular dissection of interactions between Rad51 and members of the recombination-repair group

Authors

KREJČÍ, Lumír, Jiří DAMBORSKÝ, B. THOMSEN, M. DUNO and C. BENDIXEN

Edition

Molecular and Cellular Biology, 2001, 0270-7306

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

Genetics and molecular biology

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

Impact factor

Impact factor: 9.836

RIV identification code

RIV/00216224:14310/01:00002738

Organization unit

Faculty of Science

UT WoS

000166353700026

Změněno: 13/2/2002 06:02, prof. Mgr. Jiří Damborský, Dr.

Abstract

V originále

Recombination is important for the repair of DNA damage and for chromosome segregation during meiosis; it has also been shown to participate in the regulation of cell proliferation. In the yeast Saccharomyces cerevisiae, recombination requires products of the RAD52 epistasis group. The Rad51 protein associates with the Rad51, Rad52, Rad54, and Rad55 proteins to form a dynamic complex. We describe a new strategy to screen for mutations which cause specific disruption of the interaction between certain proteins in the complex, leaving other interactions intact. This approach defines distinct protein interaction domains and protein relationships within the Rad51 complex. Alignment of the mutations onto the constructed three-dimensional model of the Rad51 protein reveal possible partially overlapping interfaces for the Rad51-Rad52 and the Rad51-Rad54 interactions. Rad51-Rad55 and Rad51-Rad51 interactions are affected by the same spectrum of mutations, indicating similarity between the two modes of binding. Finally, the detection of a subset of mutations within Rad51 which disrupt the interaction with mutant Rad52 protein but activate the interaction with Rad54 suggests that dynamic changes within the Rad51 protein may contribute to an ordered reaction process.

Links

ME 276, research and development project

Name: Racionální re-design mikrobiálních enzymů podílejících se na degradaci toxických organických polutantů

Investor: Ministry of Education, Youth and Sports of the CR, Rational re-design of microbial enzymes involved in degradation of toxic organic pollutants.

MSM 143100005, plan (intention)

Name: Strukturně-funkční vztahy biomolekul a jejich role v metabolismu

Investor: Ministry of Education, Youth and Sports of the CR, Biomolecular Structure-function Relationships and their role in the Metabolism

Citovat

KREJČÍ, Lumír, Jiří DAMBORSKÝ, B. THOMSEN, M. DUNO and C. BENDIXEN. Molecular dissection of interactions between Rad51 and members of the recombination-repair group (olecular dissection of interactions between Rad51 and members of the recombination-repair group). Molecular and Cellular Biology. 2001, vol. 21, No 3, p. 966-976. ISSN 0270-7306.

@article{346013,
   author = {Krejčí, Lumír and Damborský, Jiří and Thomsen, B. and Duno, M. and Bendixen, C.},
   article_number = {3},
   language = {eng},
   issn = {0270-7306},
   journal = {Molecular and Cellular Biology},
   title = {Molecular dissection of interactions between Rad51 and members of the recombination-repair group},
   volume = {21},
   year = {2001}
}

TY  - JOUR
ID  - 346013
AU  - Krejčí, Lumír - Damborský, Jiří - Thomsen, B. - Duno, M. - Bendixen, C.
PY  - 2001
TI  - Molecular dissection of interactions between Rad51 and members of the recombination-repair group
JF  - Molecular and Cellular Biology
VL  - 21
IS  - 3
SP  - 966
EP  - 966
SN  - 02707306
N2  - Recombination is important for the repair of DNA damage and for chromosome segregation during meiosis; it has also been shown to participate in the regulation of cell proliferation. In the yeast Saccharomyces cerevisiae, recombination requires products of the RAD52 epistasis group. The Rad51 protein associates with the Rad51, Rad52, Rad54, and Rad55 proteins to form a dynamic complex. We describe a new strategy to screen for mutations which cause specific disruption of the interaction between certain proteins in the complex, leaving other interactions intact. This approach defines distinct protein interaction domains and protein relationships within the Rad51 complex. Alignment of the mutations onto the constructed three-dimensional model of the Rad51 protein reveal possible partially overlapping interfaces for the Rad51-Rad52 and the Rad51-Rad54 interactions. Rad51-Rad55 and Rad51-Rad51 interactions are affected by the same spectrum of mutations, indicating similarity between the two modes of binding. Finally, the detection of a subset of mutations within Rad51 which disrupt the interaction with mutant Rad52 protein but activate the interaction with Rad54 suggests that dynamic changes within the Rad51 protein may contribute to an ordered reaction process.
ER  -

KREJČÍ, Lumír, Jiří DAMBORSKÝ, B. THOMSEN, M. DUNO and C. BENDIXEN. Molecular dissection of interactions between Rad51 and members of the recombination-repair group (olecular dissection of interactions between Rad51 and members of the recombination-repair group). \textit{Molecular and Cellular Biology}. 2001, vol.~21, No~3, p.~966-976. ISSN~0270-7306.

Detailed Information on Publication Record